{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Mills KB"],"funding":["NIAID NIH HHS","NIGMS NIH HHS","NIH HHS"],"pubmed_abstract":["<i>Staphylococcus aureus</i> causes the majority of skin and soft tissue infections, but this pathogen only transiently colonizes healthy skin. However, this transient skin exposure enables <i>S. aureus</i> to transition to infection. Initial adhesion of <i>S. aureus</i> to skin corneocytes is mediated by surface protein G (SasG). Here, phylogenetic analyses reveal the presence of two major divergent SasG alleles in <i>S. aureus</i>, SasG-I and SasG-II. Structural analyses of SasG-II identified a unique non-aromatic arginine in the binding pocket of the lectin subdomain that mediates adhesion to corneocytes. Atomic force microscopy and corneocyte adhesion assays indicated SasG-II can bind to a broader variety of ligands than SasG-I. Glycosidase treatment resulted in different binding profiles between SasG-I and SasG-II on skin cells. Additionally, SasG-mediated adhesion was recapitulated using differentiated N/TERT keratinocytes. Our findings indicate that SasG-II has evolved to adhere to multiple ligands, conferring a distinct advantage to <i>S. aureus</i> during skin colonization."],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2023.11.20.567970"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10690190"],"repository":["biostudies-literature"],"pubmed_title":["<i>Staphylococcus aureus</i> skin colonization is mediated by SasG lectin variation."],"pmcid":["PMC10690190"],"funding_grant_id":["R56 AI162964","R01 GM094363","P30 GM124165","S10 OD021527","R01 AI162964"],"pubmed_authors":["Fey PD","Herr AB","Maciag JJ","Dufrene YF","Crawford JA","Robinson DA","Wang C","Horswill AR","Enroth TJ","Mills KB","Keim KC"],"additional_accession":[]},"is_claimable":false,"name":"<i>Staphylococcus aureus</i> skin colonization is mediated by SasG lectin variation.","description":"<i>Staphylococcus aureus</i> causes the majority of skin and soft tissue infections, but this pathogen only transiently colonizes healthy skin. However, this transient skin exposure enables <i>S. aureus</i> to transition to infection. Initial adhesion of <i>S. aureus</i> to skin corneocytes is mediated by surface protein G (SasG). Here, phylogenetic analyses reveal the presence of two major divergent SasG alleles in <i>S. aureus</i>, SasG-I and SasG-II. Structural analyses of SasG-II identified a unique non-aromatic arginine in the binding pocket of the lectin subdomain that mediates adhesion to corneocytes. Atomic force microscopy and corneocyte adhesion assays indicated SasG-II can bind to a broader variety of ligands than SasG-I. Glycosidase treatment resulted in different binding profiles between SasG-I and SasG-II on skin cells. Additionally, SasG-mediated adhesion was recapitulated using differentiated N/TERT keratinocytes. Our findings indicate that SasG-II has evolved to adhere to multiple ligands, conferring a distinct advantage to <i>S. aureus</i> during skin colonization.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Nov","modification":"2025-09-01T03:16:44.627Z","creation":"2025-04-25T17:22:59.518Z"},"accession":"S-EPMC10690190","cross_references":{"pubmed":["38045275"],"doi":["10.1101/2023.11.20.567970"]}}